SRC mediates a switch from microtubule- to actin-based motility of vaccinia virus

Science. 2004 Oct 1;306(5693):124-9. doi: 10.1126/science.1101509. Epub 2004 Aug 5.

Abstract

The cascade of events that leads to vaccinia-induced actin polymerization requires Src-dependent tyrosine phosphorylation of the viral membrane protein A36R. We found that a localized outside-in signaling cascade induced by the viral membrane protein B5R is required to potently activate Src and induce A36R phosphorylation at the plasma membrane. In addition, Src-mediated phosphorylation of A36R regulated the ability of virus particles to recruit and release conventional kinesin. Thus, Src activity regulates the transition between cytoplasmic microtubule transport and actin-based motility at the plasma membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Animals
  • Cell Line
  • Cell Membrane / metabolism
  • Cell Membrane / virology
  • Chickens
  • Consensus Sequence
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • Kinesins / metabolism
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism
  • Microtubules / metabolism*
  • Phosphorylation
  • Phosphotyrosine / metabolism
  • Recombinant Fusion Proteins / metabolism
  • Vaccinia virus / genetics
  • Vaccinia virus / metabolism*
  • Vaccinia virus / physiology
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / metabolism
  • Viral Structural Proteins / metabolism*
  • Virion / metabolism
  • src-Family Kinases / metabolism*

Substances

  • A36R protein, Vaccinia virus
  • Actins
  • Membrane Glycoproteins
  • Recombinant Fusion Proteins
  • Viral Envelope Proteins
  • Viral Structural Proteins
  • 42kDa protein, Vaccinia virus
  • Phosphotyrosine
  • src-Family Kinases
  • Kinesins